5tq2
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in complex with zinc at GluN1 and GluN2A== | |
| - | + | <StructureSection load='5tq2' size='340' side='right' caption='[[5tq2]], [[Resolution|resolution]] 3.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5tq2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TQ2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tq0|5tq0]], [[5tpz|5tpz]], [[5tpw|5tpw]]</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tq2 OCA], [http://pdbe.org/5tq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tq2 RCSB], [http://www.ebi.ac.uk/pdbsum/5tq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tq2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NMDE1_RAT NMDE1_RAT]] NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Furukawa, H]] | ||
| + | [[Category: Karakas, E]] | ||
| + | [[Category: Romero-Hernandez, A]] | ||
| + | [[Category: Simorowski, N]] | ||
| + | [[Category: Allosteric modulation]] | ||
| + | [[Category: Ion channel]] | ||
| + | [[Category: Nmda receptor]] | ||
| + | [[Category: Transport protein]] | ||
| + | [[Category: Zinc inhibition]] | ||
Revision as of 19:22, 15 December 2016
Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in complex with zinc at GluN1 and GluN2A
| |||||||||||
